Full text data of MBOAT7
MBOAT7
(BB1, LENG4, OACT7)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Lysophospholipid acyltransferase 7; LPLAT 7; 2.3.1.- (1-acylglycerophosphatidylinositol O-acyltransferase; 2.3.1.n4; Bladder and breast carcinoma-overexpressed gene 1 protein; Leukocyte receptor cluster member 4; Lysophosphatidylinositol acyltransferase; LPIAT; Lyso-PI acyltransferase; Membrane-bound O-acyltransferase domain-containing protein 7; O-acyltransferase domain-containing protein 7; h-mboa-7)
Lysophospholipid acyltransferase 7; LPLAT 7; 2.3.1.- (1-acylglycerophosphatidylinositol O-acyltransferase; 2.3.1.n4; Bladder and breast carcinoma-overexpressed gene 1 protein; Leukocyte receptor cluster member 4; Lysophosphatidylinositol acyltransferase; LPIAT; Lyso-PI acyltransferase; Membrane-bound O-acyltransferase domain-containing protein 7; O-acyltransferase domain-containing protein 7; h-mboa-7)
Comments
Isoform Q96N66-2 was detected.
Isoform Q96N66-2 was detected.
UniProt
Q96N66
ID MBOA7_HUMAN Reviewed; 472 AA.
AC Q96N66; A9C4B6; B0V3I5; B4DQ87; Q05DF0; Q7L5N2; Q99908; Q9BPV2;
read moreAC Q9BRE9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 22-JAN-2014, entry version 82.
DE RecName: Full=Lysophospholipid acyltransferase 7;
DE Short=LPLAT 7;
DE EC=2.3.1.-;
DE AltName: Full=1-acylglycerophosphatidylinositol O-acyltransferase;
DE EC=2.3.1.n4;
DE AltName: Full=Bladder and breast carcinoma-overexpressed gene 1 protein;
DE AltName: Full=Leukocyte receptor cluster member 4;
DE AltName: Full=Lysophosphatidylinositol acyltransferase;
DE Short=LPIAT;
DE Short=Lyso-PI acyltransferase;
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 7;
DE Short=O-acyltransferase domain-containing protein 7;
DE Short=h-mboa-7;
GN Name=MBOAT7; Synonyms=BB1, LENG4, OACT7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP AND PATHWAY.
RX PubMed=18094042; DOI=10.1091/mbc.E07-09-0893;
RA Lee H.C., Inoue T., Imae R., Kono N., Shirae S., Matsuda S.,
RA Gengyo-Ando K., Mitani S., Arai H.;
RT "Caenorhabditis elegans mboa-7, a member of the MBOAT family, is
RT required for selective incorporation of polyunsaturated fatty acids
RT into phosphatidylinositol.";
RL Mol. Biol. Cell 19:1174-1184(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 2-472 (ISOFORM 1), AND VARIANT LEU-261.
RC TISSUE=Colon, Kidney, Lung, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-472 (ISOFORM 1).
RX PubMed=8702217;
RA Fukunaga-Johnson N., Lee S.W., Liebert M., Grossman H.B.;
RT "Molecular analysis of a gene, BB1, overexpressed in bladder and
RT breast carcinoma.";
RL Anticancer Res. 16:1085-1090(1996).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=18772128; DOI=10.1074/jbc.M806194200;
RA Gijon M.A., Riekhof W.R., Zarini S., Murphy R.C., Voelker D.R.;
RT "Lysophospholipid acyltransferases and arachidonate recycling in human
RT neutrophils.";
RL J. Biol. Chem. 283:30235-30245(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Acyltransferase which mediates the conversion of
CC lysophosphatidylinositol (1-acylglycerophosphatidylinositol or
CC LPI) into phosphatidylinositol (1,2-diacyl-sn-glycero-3-
CC phosphoinositol or PI) (LPIAT activity). Prefers arachidonoyl-CoA
CC as the acyl donor. Lysophospholipid acyltransferases (LPLATs)
CC catalyze the reacylation step of the phospholipid remodeling
CC pathway also known as the Lands cycle.
CC -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycero-3-
CC phosphatidylinositol = CoA + 1,2-diacyl-sn-glycero-3-
CC phosphatidylinositol.
CC -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + 1-acyl-sn-
CC glycerol 3-phosphate = [acyl-carrier-protein] + 1,2-diacyl-sn-
CC glycerol 3-phosphate.
CC -!- ENZYME REGULATION: Activity is inhibited by thimerosal.
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- INTERACTION:
CC Q86WV6:TMEM173; NbExp=2; IntAct=EBI-6116499, EBI-2800345;
CC Q8VCW4:Unc93b1 (xeno); NbExp=2; IntAct=EBI-6116499, EBI-6116986;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96N66-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96N66-2; Sequence=VSP_030967;
CC Name=3;
CC IsoId=Q96N66-3; Sequence=VSP_030968;
CC -!- TISSUE SPECIFICITY: Overexpressed in metastatic breast and bladder
CC carcinomas relative to normal breast epithelium and urothelium.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB37433.1; Type=Frameshift; Positions=63, 93, 144, 186;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; EU016381; ABV66273.1; -; mRNA.
DR EMBL; AK055908; BAB71043.1; -; mRNA.
DR EMBL; AK298689; BAG60849.1; -; mRNA.
DR EMBL; CU151838; CAQ09590.1; -; Genomic_DNA.
DR EMBL; CU151838; CAQ09591.1; -; Genomic_DNA.
DR EMBL; CU457734; CAP19119.1; -; Genomic_DNA.
DR EMBL; CU457734; CAP19120.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW72199.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW72202.1; -; Genomic_DNA.
DR EMBL; BC002512; AAH02512.2; -; mRNA.
DR EMBL; BC003164; AAH03164.2; -; mRNA.
DR EMBL; BC006309; AAH06309.1; -; mRNA.
DR EMBL; BC015857; AAH15857.1; -; mRNA.
DR EMBL; S82470; AAB37433.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001139528.1; NM_001146056.2.
DR RefSeq; NP_001139554.1; NM_001146082.2.
DR RefSeq; NP_001139555.1; NM_001146083.2.
DR RefSeq; NP_077274.3; NM_024298.4.
DR RefSeq; XP_005259302.1; XM_005259245.1.
DR RefSeq; XP_005277146.1; XM_005277089.1.
DR RefSeq; XP_005277184.1; XM_005277127.1.
DR RefSeq; XP_005277209.1; XM_005277152.1.
DR RefSeq; XP_005277231.1; XM_005277174.1.
DR RefSeq; XP_005277254.1; XM_005277197.1.
DR RefSeq; XP_005277277.1; XM_005277220.1.
DR RefSeq; XP_005277335.1; XM_005277278.1.
DR RefSeq; XP_005277377.1; XM_005277320.1.
DR RefSeq; XP_005278349.1; XM_005278292.1.
DR UniGene; Hs.467279; -.
DR ProteinModelPortal; Q96N66; -.
DR IntAct; Q96N66; 3.
DR MINT; MINT-4991231; -.
DR PhosphoSite; Q96N66; -.
DR DMDM; 167008974; -.
DR PaxDb; Q96N66; -.
DR PRIDE; Q96N66; -.
DR DNASU; 79143; -.
DR Ensembl; ENST00000245615; ENSP00000245615; ENSG00000125505.
DR Ensembl; ENST00000338624; ENSP00000344377; ENSG00000125505.
DR Ensembl; ENST00000391754; ENSP00000375634; ENSG00000125505.
DR Ensembl; ENST00000431666; ENSP00000410503; ENSG00000125505.
DR Ensembl; ENST00000570433; ENSP00000459909; ENSG00000272118.
DR Ensembl; ENST00000570701; ENSP00000460826; ENSG00000261917.
DR Ensembl; ENST00000571661; ENSP00000461840; ENSG00000261917.
DR Ensembl; ENST00000572677; ENSP00000460524; ENSG00000262053.
DR Ensembl; ENST00000572955; ENSP00000461623; ENSG00000272118.
DR Ensembl; ENST00000573438; ENSP00000459195; ENSG00000272118.
DR Ensembl; ENST00000573544; ENSP00000459183; ENSG00000261917.
DR Ensembl; ENST00000574555; ENSP00000460744; ENSG00000261917.
DR Ensembl; ENST00000574811; ENSP00000461894; ENSG00000262053.
DR Ensembl; ENST00000575098; ENSP00000459099; ENSG00000262053.
DR Ensembl; ENST00000575127; ENSP00000459731; ENSG00000262053.
DR Ensembl; ENST00000576648; ENSP00000459249; ENSG00000272118.
DR Ensembl; ENST00000603418; ENSP00000474282; ENSG00000271019.
DR Ensembl; ENST00000603936; ENSP00000475017; ENSG00000271019.
DR Ensembl; ENST00000605719; ENSP00000473695; ENSG00000271019.
DR Ensembl; ENST00000605770; ENSP00000474492; ENSG00000271019.
DR Ensembl; ENST00000606211; ENSP00000475388; ENSG00000271733.
DR Ensembl; ENST00000606335; ENSP00000475976; ENSG00000271908.
DR Ensembl; ENST00000606614; ENSP00000475193; ENSG00000271744.
DR Ensembl; ENST00000606678; ENSP00000476011; ENSG00000272513.
DR Ensembl; ENST00000606734; ENSP00000475964; ENSG00000271744.
DR Ensembl; ENST00000606746; ENSP00000476069; ENSG00000271733.
DR Ensembl; ENST00000606768; ENSP00000475614; ENSG00000271791.
DR Ensembl; ENST00000606836; ENSP00000475500; ENSG00000271908.
DR Ensembl; ENST00000606981; ENSP00000475878; ENSG00000271791.
DR Ensembl; ENST00000606984; ENSP00000475163; ENSG00000271908.
DR Ensembl; ENST00000607069; ENSP00000475618; ENSG00000271733.
DR Ensembl; ENST00000607123; ENSP00000475735; ENSG00000271744.
DR Ensembl; ENST00000607143; ENSP00000475230; ENSG00000272513.
DR Ensembl; ENST00000607209; ENSP00000475839; ENSG00000272513.
DR Ensembl; ENST00000607243; ENSP00000475210; ENSG00000271908.
DR Ensembl; ENST00000607354; ENSP00000476108; ENSG00000271733.
DR Ensembl; ENST00000607477; ENSP00000476182; ENSG00000272513.
DR Ensembl; ENST00000607667; ENSP00000475821; ENSG00000271791.
DR Ensembl; ENST00000607717; ENSP00000475597; ENSG00000271791.
DR Ensembl; ENST00000607767; ENSP00000475323; ENSG00000271744.
DR GeneID; 79143; -.
DR KEGG; hsa:79143; -.
DR UCSC; uc002qdq.3; human.
DR CTD; 79143; -.
DR GeneCards; GC19M054677; -.
DR HGNC; HGNC:15505; MBOAT7.
DR HPA; HPA055967; -.
DR MIM; 606048; gene.
DR neXtProt; NX_Q96N66; -.
DR PharmGKB; PA162395057; -.
DR eggNOG; COG5202; -.
DR HOVERGEN; HBG105712; -.
DR InParanoid; Q96N66; -.
DR KO; K13516; -.
DR OMA; WTFLYLL; -.
DR PhylomeDB; Q96N66; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00085; -.
DR ChiTaRS; MBOAT7; human.
DR GenomeRNAi; 79143; -.
DR NextBio; 68029; -.
DR PRO; PR:Q96N66; -.
DR ArrayExpress; Q96N66; -.
DR Bgee; Q96N66; -.
DR CleanEx; HS_MBOAT7; -.
DR Genevestigator; Q96N66; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:UniProtKB-EC.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; TAS:Reactome.
DR GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0021591; P:ventricular system development; IEA:Ensembl.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Complete proteome;
KW Glycoprotein; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Polymorphism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 472 Lysophospholipid acyltransferase 7.
FT /FTId=PRO_0000317457.
FT TRANSMEM 9 29 Helical; (Potential).
FT TRANSMEM 44 64 Helical; (Potential).
FT TRANSMEM 74 94 Helical; (Potential).
FT TRANSMEM 197 217 Helical; (Potential).
FT TRANSMEM 247 267 Helical; (Potential).
FT TRANSMEM 355 375 Helical; (Potential).
FT TRANSMEM 429 449 Helical; (Potential).
FT CARBOHYD 321 321 N-linked (GlcNAc...) (Potential).
FT VAR_SEQ 1 111 MSPEEWTYLVVLLISIPIGFLFKKAGPGLKRWGAAAVGLGL
FT TLFTCGPHTLHSLVTILGTWALIQAQPCSCHALALAWTFSY
FT LLFFRALSLLGLPTPTPFTNAVQLLLTLK -> MGSSRCGP
FT GAHPVHLWPPHFAFSGHHPRDLGPHSGPAL (in
FT isoform 2).
FT /FTId=VSP_030967.
FT VAR_SEQ 345 472 Missing (in isoform 3).
FT /FTId=VSP_030968.
FT VARIANT 261 261 F -> L (in dbSNP:rs17855385).
FT /FTId=VAR_038526.
FT VARIANT 415 415 V -> L (in dbSNP:rs35909464).
FT /FTId=VAR_038527.
FT CONFLICT 70 70 S -> P (in Ref. 2; BAB71043).
FT CONFLICT 345 345 S -> T (in Ref. 6; AAB37433).
SQ SEQUENCE 472 AA; 52765 MW; 1743F924468D3D2D CRC64;
MSPEEWTYLV VLLISIPIGF LFKKAGPGLK RWGAAAVGLG LTLFTCGPHT LHSLVTILGT
WALIQAQPCS CHALALAWTF SYLLFFRALS LLGLPTPTPF TNAVQLLLTL KLVSLASEVQ
DLHLAQRKEM ASGFSKGPTL GLLPDVPSLM ETLSYSYCYV GIMTGPFFRY RTYLDWLEQP
FPGAVPSLRP LLRRAWPAPL FGLLFLLSSH LFPLEAVRED AFYARPLPAR LFYMIPVFFA
FRMRFYVAWI AAECGCIAAG FGAYPVAAKA RAGGGPTLQC PPPSSPEKAA SLEYDYETIR
NIDCYSTDFC VRVRDGMRYW NMTVQWWLAQ YIYKSAPARS YVLRSAWTML LSAYWHGLHP
GYYLSFLTIP LCLAAEGRLE SALRGRLSPG GQKAWDWVHW FLKMRAYDYM CMGFVLLSLA
DTLRYWASIY FCIHFLALAA LGLGLALGGG SPSRRKAASQ PTSLAPEKLR EE
//
ID MBOA7_HUMAN Reviewed; 472 AA.
AC Q96N66; A9C4B6; B0V3I5; B4DQ87; Q05DF0; Q7L5N2; Q99908; Q9BPV2;
read moreAC Q9BRE9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 22-JAN-2014, entry version 82.
DE RecName: Full=Lysophospholipid acyltransferase 7;
DE Short=LPLAT 7;
DE EC=2.3.1.-;
DE AltName: Full=1-acylglycerophosphatidylinositol O-acyltransferase;
DE EC=2.3.1.n4;
DE AltName: Full=Bladder and breast carcinoma-overexpressed gene 1 protein;
DE AltName: Full=Leukocyte receptor cluster member 4;
DE AltName: Full=Lysophosphatidylinositol acyltransferase;
DE Short=LPIAT;
DE Short=Lyso-PI acyltransferase;
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 7;
DE Short=O-acyltransferase domain-containing protein 7;
DE Short=h-mboa-7;
GN Name=MBOAT7; Synonyms=BB1, LENG4, OACT7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP AND PATHWAY.
RX PubMed=18094042; DOI=10.1091/mbc.E07-09-0893;
RA Lee H.C., Inoue T., Imae R., Kono N., Shirae S., Matsuda S.,
RA Gengyo-Ando K., Mitani S., Arai H.;
RT "Caenorhabditis elegans mboa-7, a member of the MBOAT family, is
RT required for selective incorporation of polyunsaturated fatty acids
RT into phosphatidylinositol.";
RL Mol. Biol. Cell 19:1174-1184(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 2-472 (ISOFORM 1), AND VARIANT LEU-261.
RC TISSUE=Colon, Kidney, Lung, and Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-472 (ISOFORM 1).
RX PubMed=8702217;
RA Fukunaga-Johnson N., Lee S.W., Liebert M., Grossman H.B.;
RT "Molecular analysis of a gene, BB1, overexpressed in bladder and
RT breast carcinoma.";
RL Anticancer Res. 16:1085-1090(1996).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=18772128; DOI=10.1074/jbc.M806194200;
RA Gijon M.A., Riekhof W.R., Zarini S., Murphy R.C., Voelker D.R.;
RT "Lysophospholipid acyltransferases and arachidonate recycling in human
RT neutrophils.";
RL J. Biol. Chem. 283:30235-30245(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Acyltransferase which mediates the conversion of
CC lysophosphatidylinositol (1-acylglycerophosphatidylinositol or
CC LPI) into phosphatidylinositol (1,2-diacyl-sn-glycero-3-
CC phosphoinositol or PI) (LPIAT activity). Prefers arachidonoyl-CoA
CC as the acyl donor. Lysophospholipid acyltransferases (LPLATs)
CC catalyze the reacylation step of the phospholipid remodeling
CC pathway also known as the Lands cycle.
CC -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycero-3-
CC phosphatidylinositol = CoA + 1,2-diacyl-sn-glycero-3-
CC phosphatidylinositol.
CC -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + 1-acyl-sn-
CC glycerol 3-phosphate = [acyl-carrier-protein] + 1,2-diacyl-sn-
CC glycerol 3-phosphate.
CC -!- ENZYME REGULATION: Activity is inhibited by thimerosal.
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC -!- INTERACTION:
CC Q86WV6:TMEM173; NbExp=2; IntAct=EBI-6116499, EBI-2800345;
CC Q8VCW4:Unc93b1 (xeno); NbExp=2; IntAct=EBI-6116499, EBI-6116986;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96N66-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96N66-2; Sequence=VSP_030967;
CC Name=3;
CC IsoId=Q96N66-3; Sequence=VSP_030968;
CC -!- TISSUE SPECIFICITY: Overexpressed in metastatic breast and bladder
CC carcinomas relative to normal breast epithelium and urothelium.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB37433.1; Type=Frameshift; Positions=63, 93, 144, 186;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; EU016381; ABV66273.1; -; mRNA.
DR EMBL; AK055908; BAB71043.1; -; mRNA.
DR EMBL; AK298689; BAG60849.1; -; mRNA.
DR EMBL; CU151838; CAQ09590.1; -; Genomic_DNA.
DR EMBL; CU151838; CAQ09591.1; -; Genomic_DNA.
DR EMBL; CU457734; CAP19119.1; -; Genomic_DNA.
DR EMBL; CU457734; CAP19120.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW72199.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW72202.1; -; Genomic_DNA.
DR EMBL; BC002512; AAH02512.2; -; mRNA.
DR EMBL; BC003164; AAH03164.2; -; mRNA.
DR EMBL; BC006309; AAH06309.1; -; mRNA.
DR EMBL; BC015857; AAH15857.1; -; mRNA.
DR EMBL; S82470; AAB37433.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001139528.1; NM_001146056.2.
DR RefSeq; NP_001139554.1; NM_001146082.2.
DR RefSeq; NP_001139555.1; NM_001146083.2.
DR RefSeq; NP_077274.3; NM_024298.4.
DR RefSeq; XP_005259302.1; XM_005259245.1.
DR RefSeq; XP_005277146.1; XM_005277089.1.
DR RefSeq; XP_005277184.1; XM_005277127.1.
DR RefSeq; XP_005277209.1; XM_005277152.1.
DR RefSeq; XP_005277231.1; XM_005277174.1.
DR RefSeq; XP_005277254.1; XM_005277197.1.
DR RefSeq; XP_005277277.1; XM_005277220.1.
DR RefSeq; XP_005277335.1; XM_005277278.1.
DR RefSeq; XP_005277377.1; XM_005277320.1.
DR RefSeq; XP_005278349.1; XM_005278292.1.
DR UniGene; Hs.467279; -.
DR ProteinModelPortal; Q96N66; -.
DR IntAct; Q96N66; 3.
DR MINT; MINT-4991231; -.
DR PhosphoSite; Q96N66; -.
DR DMDM; 167008974; -.
DR PaxDb; Q96N66; -.
DR PRIDE; Q96N66; -.
DR DNASU; 79143; -.
DR Ensembl; ENST00000245615; ENSP00000245615; ENSG00000125505.
DR Ensembl; ENST00000338624; ENSP00000344377; ENSG00000125505.
DR Ensembl; ENST00000391754; ENSP00000375634; ENSG00000125505.
DR Ensembl; ENST00000431666; ENSP00000410503; ENSG00000125505.
DR Ensembl; ENST00000570433; ENSP00000459909; ENSG00000272118.
DR Ensembl; ENST00000570701; ENSP00000460826; ENSG00000261917.
DR Ensembl; ENST00000571661; ENSP00000461840; ENSG00000261917.
DR Ensembl; ENST00000572677; ENSP00000460524; ENSG00000262053.
DR Ensembl; ENST00000572955; ENSP00000461623; ENSG00000272118.
DR Ensembl; ENST00000573438; ENSP00000459195; ENSG00000272118.
DR Ensembl; ENST00000573544; ENSP00000459183; ENSG00000261917.
DR Ensembl; ENST00000574555; ENSP00000460744; ENSG00000261917.
DR Ensembl; ENST00000574811; ENSP00000461894; ENSG00000262053.
DR Ensembl; ENST00000575098; ENSP00000459099; ENSG00000262053.
DR Ensembl; ENST00000575127; ENSP00000459731; ENSG00000262053.
DR Ensembl; ENST00000576648; ENSP00000459249; ENSG00000272118.
DR Ensembl; ENST00000603418; ENSP00000474282; ENSG00000271019.
DR Ensembl; ENST00000603936; ENSP00000475017; ENSG00000271019.
DR Ensembl; ENST00000605719; ENSP00000473695; ENSG00000271019.
DR Ensembl; ENST00000605770; ENSP00000474492; ENSG00000271019.
DR Ensembl; ENST00000606211; ENSP00000475388; ENSG00000271733.
DR Ensembl; ENST00000606335; ENSP00000475976; ENSG00000271908.
DR Ensembl; ENST00000606614; ENSP00000475193; ENSG00000271744.
DR Ensembl; ENST00000606678; ENSP00000476011; ENSG00000272513.
DR Ensembl; ENST00000606734; ENSP00000475964; ENSG00000271744.
DR Ensembl; ENST00000606746; ENSP00000476069; ENSG00000271733.
DR Ensembl; ENST00000606768; ENSP00000475614; ENSG00000271791.
DR Ensembl; ENST00000606836; ENSP00000475500; ENSG00000271908.
DR Ensembl; ENST00000606981; ENSP00000475878; ENSG00000271791.
DR Ensembl; ENST00000606984; ENSP00000475163; ENSG00000271908.
DR Ensembl; ENST00000607069; ENSP00000475618; ENSG00000271733.
DR Ensembl; ENST00000607123; ENSP00000475735; ENSG00000271744.
DR Ensembl; ENST00000607143; ENSP00000475230; ENSG00000272513.
DR Ensembl; ENST00000607209; ENSP00000475839; ENSG00000272513.
DR Ensembl; ENST00000607243; ENSP00000475210; ENSG00000271908.
DR Ensembl; ENST00000607354; ENSP00000476108; ENSG00000271733.
DR Ensembl; ENST00000607477; ENSP00000476182; ENSG00000272513.
DR Ensembl; ENST00000607667; ENSP00000475821; ENSG00000271791.
DR Ensembl; ENST00000607717; ENSP00000475597; ENSG00000271791.
DR Ensembl; ENST00000607767; ENSP00000475323; ENSG00000271744.
DR GeneID; 79143; -.
DR KEGG; hsa:79143; -.
DR UCSC; uc002qdq.3; human.
DR CTD; 79143; -.
DR GeneCards; GC19M054677; -.
DR HGNC; HGNC:15505; MBOAT7.
DR HPA; HPA055967; -.
DR MIM; 606048; gene.
DR neXtProt; NX_Q96N66; -.
DR PharmGKB; PA162395057; -.
DR eggNOG; COG5202; -.
DR HOVERGEN; HBG105712; -.
DR InParanoid; Q96N66; -.
DR KO; K13516; -.
DR OMA; WTFLYLL; -.
DR PhylomeDB; Q96N66; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00085; -.
DR ChiTaRS; MBOAT7; human.
DR GenomeRNAi; 79143; -.
DR NextBio; 68029; -.
DR PRO; PR:Q96N66; -.
DR ArrayExpress; Q96N66; -.
DR Bgee; Q96N66; -.
DR CleanEx; HS_MBOAT7; -.
DR Genevestigator; Q96N66; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:UniProtKB-EC.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; TAS:Reactome.
DR GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0021591; P:ventricular system development; IEA:Ensembl.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Complete proteome;
KW Glycoprotein; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Polymorphism;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1 472 Lysophospholipid acyltransferase 7.
FT /FTId=PRO_0000317457.
FT TRANSMEM 9 29 Helical; (Potential).
FT TRANSMEM 44 64 Helical; (Potential).
FT TRANSMEM 74 94 Helical; (Potential).
FT TRANSMEM 197 217 Helical; (Potential).
FT TRANSMEM 247 267 Helical; (Potential).
FT TRANSMEM 355 375 Helical; (Potential).
FT TRANSMEM 429 449 Helical; (Potential).
FT CARBOHYD 321 321 N-linked (GlcNAc...) (Potential).
FT VAR_SEQ 1 111 MSPEEWTYLVVLLISIPIGFLFKKAGPGLKRWGAAAVGLGL
FT TLFTCGPHTLHSLVTILGTWALIQAQPCSCHALALAWTFSY
FT LLFFRALSLLGLPTPTPFTNAVQLLLTLK -> MGSSRCGP
FT GAHPVHLWPPHFAFSGHHPRDLGPHSGPAL (in
FT isoform 2).
FT /FTId=VSP_030967.
FT VAR_SEQ 345 472 Missing (in isoform 3).
FT /FTId=VSP_030968.
FT VARIANT 261 261 F -> L (in dbSNP:rs17855385).
FT /FTId=VAR_038526.
FT VARIANT 415 415 V -> L (in dbSNP:rs35909464).
FT /FTId=VAR_038527.
FT CONFLICT 70 70 S -> P (in Ref. 2; BAB71043).
FT CONFLICT 345 345 S -> T (in Ref. 6; AAB37433).
SQ SEQUENCE 472 AA; 52765 MW; 1743F924468D3D2D CRC64;
MSPEEWTYLV VLLISIPIGF LFKKAGPGLK RWGAAAVGLG LTLFTCGPHT LHSLVTILGT
WALIQAQPCS CHALALAWTF SYLLFFRALS LLGLPTPTPF TNAVQLLLTL KLVSLASEVQ
DLHLAQRKEM ASGFSKGPTL GLLPDVPSLM ETLSYSYCYV GIMTGPFFRY RTYLDWLEQP
FPGAVPSLRP LLRRAWPAPL FGLLFLLSSH LFPLEAVRED AFYARPLPAR LFYMIPVFFA
FRMRFYVAWI AAECGCIAAG FGAYPVAAKA RAGGGPTLQC PPPSSPEKAA SLEYDYETIR
NIDCYSTDFC VRVRDGMRYW NMTVQWWLAQ YIYKSAPARS YVLRSAWTML LSAYWHGLHP
GYYLSFLTIP LCLAAEGRLE SALRGRLSPG GQKAWDWVHW FLKMRAYDYM CMGFVLLSLA
DTLRYWASIY FCIHFLALAA LGLGLALGGG SPSRRKAASQ PTSLAPEKLR EE
//
MIM
606048
*RECORD*
*FIELD* NO
606048
*FIELD* TI
*606048 LEUKOCYTE RECEPTOR CLUSTER GENE 4; LENG4
;;BREAST AND BLADDER CANCER OVEREXPRESSED GENE 1; BB1
read more*FIELD* TX
CLONING
Overexpression of genes is one of the genetic alterations that may have
a role in the development and progression of cancers. By immunoscreening
a bladder tumor cell cDNA expression library with antibody to AN43, a
bladder tumor-associated antigen, Fukunaga-Johnson et al. (1996)
isolated a cDNA encoding BB1. The deduced 343-amino acid protein
contains both hydrophilic and hydrophobic regions, suggesting that it
may be a transmembrane protein. Northern blot analysis revealed elevated
expression of a 2.0-kb transcript in breast and bladder tumor cells
compared with normal cells. Expression in the cancer cells could be
reduced by treatment with gamma-interferon (IFNG; 147570). Because of a
lack of reactivity of the expressed BB1 protein on Western blots,
Fukunaga-Johnson et al. (1996) concluded that BB1 is distinct from the
AN43 antigen.
MAPPING
By genomic sequence analysis, Wende et al. (2000) mapped the BB1 gene,
which they termed LENG4, to 19q13.4. They noted that the LENG genes,
unlike other genes in the leukocyte receptor cluster on 19q13.4, do not
encode proteins with immunoglobulin domains.
*FIELD* RF
1. Fukunaga-Johnson, N.; Lee, S. W.; Liebert, M.; Grossman, H. B.
: Molecular analysis of a gene, BB1, overexpressed in bladder and
breast carcinoma. Anticancer Res. 16: 1085-1090, 1996.
2. Wende, H.; Volz, A.; Ziegler, A.: Extensive gene duplications
and a large inversion characterize the human leukocyte receptor cluster. Immunogenetics 51:
703-713, 2000. Note: Erratum: Immunogenetics 52: 308 only, 2001.
*FIELD* CD
Paul J. Converse: 6/20/2001
*FIELD* ED
alopez: 12/20/2006
mgross: 8/30/2005
mgross: 6/20/2001
*RECORD*
*FIELD* NO
606048
*FIELD* TI
*606048 LEUKOCYTE RECEPTOR CLUSTER GENE 4; LENG4
;;BREAST AND BLADDER CANCER OVEREXPRESSED GENE 1; BB1
read more*FIELD* TX
CLONING
Overexpression of genes is one of the genetic alterations that may have
a role in the development and progression of cancers. By immunoscreening
a bladder tumor cell cDNA expression library with antibody to AN43, a
bladder tumor-associated antigen, Fukunaga-Johnson et al. (1996)
isolated a cDNA encoding BB1. The deduced 343-amino acid protein
contains both hydrophilic and hydrophobic regions, suggesting that it
may be a transmembrane protein. Northern blot analysis revealed elevated
expression of a 2.0-kb transcript in breast and bladder tumor cells
compared with normal cells. Expression in the cancer cells could be
reduced by treatment with gamma-interferon (IFNG; 147570). Because of a
lack of reactivity of the expressed BB1 protein on Western blots,
Fukunaga-Johnson et al. (1996) concluded that BB1 is distinct from the
AN43 antigen.
MAPPING
By genomic sequence analysis, Wende et al. (2000) mapped the BB1 gene,
which they termed LENG4, to 19q13.4. They noted that the LENG genes,
unlike other genes in the leukocyte receptor cluster on 19q13.4, do not
encode proteins with immunoglobulin domains.
*FIELD* RF
1. Fukunaga-Johnson, N.; Lee, S. W.; Liebert, M.; Grossman, H. B.
: Molecular analysis of a gene, BB1, overexpressed in bladder and
breast carcinoma. Anticancer Res. 16: 1085-1090, 1996.
2. Wende, H.; Volz, A.; Ziegler, A.: Extensive gene duplications
and a large inversion characterize the human leukocyte receptor cluster. Immunogenetics 51:
703-713, 2000. Note: Erratum: Immunogenetics 52: 308 only, 2001.
*FIELD* CD
Paul J. Converse: 6/20/2001
*FIELD* ED
alopez: 12/20/2006
mgross: 8/30/2005
mgross: 6/20/2001